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Literature summary for 1.8.1.7 extracted from
- Glutathione reductase from human erythrocytes. Molecular weight, subunit composition and aggregation properties (1975), Eur. J. Biochem., 60, 459-466.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
2 * 50000, SDS-PAGE | Homo sapiens |
| 96000 | - |
apoenzyme without FAD, sedimentation equilibrium | Homo sapiens |
| 100000 | - |
sedimentation equilibrium | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GSSG + NADPH | - |
Homo sapiens | glutathione + NADP+ | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 50000, SDS-PAGE | Homo sapiens |
| More | in absence of thiols, glutathione reductase shows a tendency to form tetramers and larger aggregates, catalytically active | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | FAD enzyme | Homo sapiens | |
| NADPH | - |
Homo sapiens | |
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